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Aac 00498-22
Aac 00498-22
George A. Jacoby
20 September 1932–14 February 2022
AAC Editor in Chief, 1995–2000
It is with great fondness that we remember George A. Jacoby, a colleague, a friend, Copyright © 2022 American Society for
Microbiology. All Rights Reserved.
and a giant in the area of antibacterial drug resistance. George was born in Michigan
Address correspondence to Karen Bush,
but lived most of his life in New England. He completed his undergraduate studies at karbush@indiana.edu.
Yale University and then trained at Harvard Medical School (HMS), Massachusetts The authors declare no conflict of interest.
General Hospital (MGH), the National Institutes of Health, and the National Institute for Published 4 May 2022
Medical Research at Mill Hill before joining the Infectious Diseases Unit at MGH, where
he was on the faculty for 25 years. He was an associate professor of medicine at HMS,
where he taught students for over 40 years. In 1993 he moved to the Lahey Clinic in
Burlington, MA, where he headed the Infectious Disease Department. Although he
retired from clinical work in 2002, he continued to maintain a laboratory where he
studied the genetics and biochemistry of bacterial resistance to antibiotics, especially
quinolones and b -lactams. George was a member of multiple editorial boards for a va-
riety of biochemical and medical journals, including the New England Journal of
Medicine and Antimicrobial Agents and Chemotherapy. One of the roles for which he
was most noted was that of editor-in-chief of AAC from 1995–2000. Many of us who
worked with him as an editor, as a member of the AAC Editorial Board, or as an ad hoc
reviewer recognized him as a fair and impartial advocate for good science who could
overlook occasional grammatical errors in international contributions if the science
was sound. He was noted for his speed and accuracy as an editor, a role in which he
took great pride. His comments to authors were often laced with his quiet humor amid
the constructive criticism that made all of our papers better.
George’s contributions to our understanding of antibiotic resistance are broad and
unrivaled, with collaborations established across international borders as well as across
antibiotic classes. When he began working on b -lactamases in 1963 (1), he likely did
not realize the impact he would make on this research area. His publications in the
early 1970s recognized the potential for widespread dissemination of antibiotic resist-
ance due to the mobility of R factors that carried antibiotic resistance genes (2, 3). He
described plasmid-encoded R factors in Pseudomonas aeruginosa responsible for resist-
ance to aminoglycosides and penicillins, leading to his increased attention to b -lacta-
mases. His work on identification of new b -lactamases included studies on the OXA
family of enzymes; he studied the oxacillin-hydrolyzing PSE-2 b -lactamase in the early
1980s in a collaboration with Alain Philippon (4), followed by the molecular classifica-
tion of this enzyme as a member of a fourth molecular class of b -lactamases, i.e., Class
D, together with Pentti Huovinen (5). His laboratory was the first to recognize the exis-
tence of extended-spectrum b -lactamases (ESBLs) in the United States (6). His 2009
review of AmpC b -lactamases remains one of the most readable and authoritative
compilations for that set of enzymes (7). In addition to his many contributions to the
study of b -lactamases, he was a pioneer in the first recognition of plasmid-encoded
quinolone resistance in Gram-negative bacteria, with the identification of the qnr gene
in ESBL-producing enteric bacteria (8). In collaboration with David Hooper, he identi-
fied and studied multiple plasmid-mediated quinolone resistance genes for over 20
years (9). He claimed that his interest in quinolone resistance overshadowed his b -lac-
tamase work at the end of his career, as he continued to contribute to David Hooper’s
group into early 2022.
One of his greatest contributions was his attention to antibiotic resistance nomen-
clature. During his tenure as AAC editor-in-chief, the b -lactamase community was deal-
ing with serious issues concerning the naming of new enzymes. George, together with
Karen Bush and Antone Medeiros, published a functional classification scheme for all
the known unique b -lactamases in 1995 in an AAC Minireview that for many years was
the most cited publication in the journal (10). However, many more enzymes were yet
to be identified as nucleotide sequencing became easier and cheaper, resulting in du-
plicative naming of the many new ESBLS that were being identified worldwide.
Following a b -lactamase symposium at the 1996 ICAAC meeting, representatives from
the b -lactamase community requested that George serve as the arbitrator for assign-
ing names to new b -lactamases. He then established a widely-referenced website sup-
ported by the Lahey Clinic, lahey.org/studies/, with the original intention to adjudicate
the naming of ESBLs. From 1997–2015, this website expanded to become the authori-
tative source for the naming of not only all new b -lactamases, but also for the naming
of the scores of qnr genes and gene products later identified. George retained the
curation of the Lahey database through mid-2015, with the exception of a few months
in the winter when he would retreat to Florida, where he claimed not to have sufficient
REFERENCES
1. Bush K, Jacoby GA. 2010. Updated functional classification of b -lactamases. 6. Jacoby GA, Medeiros AA, O'Brien TF, Pinto ME, Jiang H. 1988. Broad-spec-
Antimicrob Agents Chemother 54:969–976. https://doi.org/10.1128/AAC trum, transmissible b -lactamases. N Engl J Med 319:723–723.
.01009-09. 7. Jacoby GA. 2009. AmpC b -lactamases. Clin Microbiol Rev 22:161–182.
2. Jacoby GA, Sutton L. 1979. Activity of b -lactam antibiotics against Pseudomo- https://doi.org/10.1128/cmr.00036-08.
nas aeruginosa carrying R plasmids determining different b -lactamases. Anti- 8. Martínez-Martínez L, Pascual A, Jacoby G. 1998. Quinolone resistance from
microb Agents Chemother 16:243–245. https://doi.org/10.1128/AAC.16.2 a transferable plasmid. Lancet 351:797–799. https://doi.org/10.1016/S0140
.243. -6736(97)07322-4.
3. Jacoby GA. 1974. Properties of R plasmids determining gentamicin resist-
9. Hooper DC, Jacoby GA. 2015. Mechanisms of drug resistance: quinolone re-
ance by acetylation in Pseudomonas aeruginosa. Antimicrob Agents Che-
sistance. Ann N Y Acad Sci 1354:12–31. https://doi.org/10.1111/nyas.12830.
mother 6:239–252. https://doi.org/10.1128/AAC.6.3.239.
4. Philippon AM, Paul GC, Jacoby GA. 1983. Properties of PSE-2 beta-lacta- 10. Bush K, Jacoby GA, Medeiros AA. 1995. A functional classification scheme
mase and genetic basis for its production in Pseudomonas aeruginosa. for b -lactamases and its correlation with molecular structure. Antimicrob
Antimicrob Agents Chemother 24:362–369. https://doi.org/10.1128/AAC Agents Chemother 39:1211–1233. https://doi.org/10.1128/aac.39.6.1211.
.24.3.362. 11. Bradford P, Bonomo R, Bush K, Carattoli A, Feldgarden M, Haft D, Ishii Y,
5. Huovinen P, Huovinen S, Jacoby GA. 1988. Sequence of PSE-2 b -lactamase. Jacoby G, Klimke W, Palzkill T, Poirel L, Rossolini GM, Tamma P, Arias C.
Antimicrob Agents Chemother 32:134–136. https://doi.org/10.1128/AAC.32 2022. Consensus on b -lactamase nomenclature. Antimicrob Agents Che-
.1.134. mother 66:4. https://doi.org/10.1128/aac.00333-22.